Glucose-conjugated chicken myofibrillar proteins derived from random-centroid optimization present potent hydroxyl radical scavenging activity.

The optimal conditions for the preparation of glucose-conjugated chicken myofibrillar proteins (Mfs) the Maillard reaction, presenting strong antioxidant activity against hydroxyl radicals (･OH) and high solubility in low ionic strength medium, were sought using random-centroid optimization (RCO). Four parameters of temperature, relative humidity (RH), reaction time, and glucose-to-Mfs mixing ratio, were examined, resulting in a total of 24 vertices. Evaluations were carried out relatively to each individual vertex, and the optimal preparatory conditions to obtain the highest antioxidant activity were determined as follows: temperature of 52 °C, RH of 38%, reaction time of 6.

Antioxidative ability of chicken myofibrillar protein developed by glycosylation and changes in the solubility and thermal stability.

Myofibrillar protein prepared from chicken breast muscle was incubated with several concentrations of glucose or maltose for 6 h at 60 °C and 35% relative humidity in order to obtain glycosylated chicken protein. When the ratio of the weights of the myofibrillar protein and glucose or maltose had respectively reached 1:6 or 1:3-5, the solubility of each type of glycosylated chicken protein in a 0.1 M NaCl solution was exceeded by about 60%, although the myofibrillar protein was insoluble in a low ionic strength solution.

Relationship between endogenous protein disulfide isomerase family proteins and glutenin macropolymer.

The effects of endogenous protein disulfide isomerase (PDI) family proteins on the properties of gluten proteins in dough during breadmaking were determined using bacitracin, an inhibitor of PDI. Bread loaf volume in the presence of bacitracin was increased to 118% of that in the absence of bacitracin. The addition of bacitracin caused a decrease in the extension tolerance of the dough.

Rennet-induced aggregation and curd formation from skimmed milk powders prepared under different sterilizing conditions.

Heat treatment during the production of skimmed milk powder causes denaturation of proteins, thereby affecting the physicochemical properties of the skimmed milk powder. To understand the effects of heat treatment on the sensitivity of the casein micelles in skimmed milk powders, low heating type (L), normal heating type (N), high heating type (H), and super-high heating type (SH), to reaction with rennet, rennet-induced curd formation was investigated. A well-developed network structure with wide spaces was observed only in the curd derived from the solution of type L skimmed milk powder.

Action of ascorbic acid on a myosin molecule derived from carp.

The influence of L-ascorbic acid at 40 degrees C incubation on the subfragment-1 and rod regions, prepared by chymotryptic digestion of myosin, and myosin was investigated by SDS-polyacrylamide gel electrophoresis and transmission electron microscopy respectively. It was observed that L-ascorbic acid acted more readily on the subfragment-1 region of myosin. Further, circular dichroism measurement indicated that L-ascorbic acid did not affect the structure of myosin.

[Acute hemorrhagic colitis induced by the neuraminidase inhibitor oseltamivir].

A 23-year-old woman had lower abdominal pain, diarrhea and bloody stool was admitted and given a diagnosis of influenza B. Her home doctor had started treatment by neuraminidase inhibitor (oseltamivir) the previous day. Colonoscopic examination revealed an area of hemorrhage and erosion in the left transverse colon.

Beneficial effects of ascorbic acid on heat-induced fish gel (Kamaboko) from the superoxide anion radical.

We examined the participation of the superoxide anion radical (O(2)(-)) in the beneficial effects of L-ascorbic acid on heat-induced fish gel (Kamaboko). The generation of a thiyl radical (S.) in glutathione, ovalbumin, and actomyosin was examined by electron spin resonance spectroscopy coupled with spin trapping.